Abstract
It has been ten years since publication of the finding that outer membranes isolated from mitochondria of the fungus Neurospora crassa may bear periodic arrays of stain-accumulating subunits, which were later identified as the voltage-dependent anion-selective channel, VDAC (Mannella, 1982). In the ensuing years, considerable progress has been made both in controlling the crystallization process and in characterizing the structure of the arrays. The aim of the present report is to summarize information about the structure of the VDAC channel that has been obtained from high-resolution electron microscopy and image analysis of these two-dimensional (2D) crystals.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Akiba T, Yoshimura H, Namba K (1991) Monolayer crystallization of flagellar L-P rings by sequential addition and depletion of lipid. Science 252: 15444546
Blachly-Dyson E, Peng S Z, Colombini M, Forte M (1990) Selectivity changes in site-directed mutants of the VDAC ion channel: structural implications. Science 247: 1233–1236
Bowen K A, Tarn K, Colombini M (1985) Evidence for titratable gating charges controlling the voltage dependence of the outer mitochondrial membrane channel, VDAC. J Membr Biol 86: 51–59
Cox J A, Conte M, Fitton J E, DeGrado W F (1985) The interaction of calmodulin with amphiphilic peptides. J Biol Chem 260: 2527–2534
Deisenhofer J, Epp O, Miki K, Huber R, Michel H (1984) X-ray structure analysis of a membrane protein complex. Electron density map at 3A resolution and a model of the chromophores of the photosynthetic reaction center from Rhodopseudomonas viridis. J Mol Biol 180: 385–398
Forte M, Guy H R, Mannella C A (1987) Molecular genetics of the VDAC ion channel: structural model and sequence analysis. J Bioenerg Bio-membr 19: 341–350
Guo X W, Mannella C A (1992) Classification of projection images of crystalline arrays of the mitochondrial channel, VDAC, embedded in aurothioglucose. Biophys J 63, 418–427
Guo X W, Smith P R, Radermacher M, Mannella C A (1992) Structure of crystalline VDAC, the voltage-gated channel in the mitochondrial outer membrane. In: Proc. 50th Annual Meeting of the Electron Microscopy Society of America. Bailey G W, Bentley J, Small J A (eds) San Francisco Press, Inc. San Francisco, p. 440–441
Henderson R, Baldwin J M, Ceska T A, Zemlin F, Beckmann E, Downing K H (1990) Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J Mol Biol 213: 899–929
Jap B K, Walian P J, Gehring K (1991) Structural architecture of an outer membrane channel as determinined by electron crystallography. Nature 350: 167–170
Jordi W, De Kruijff B, Marsh D (1989) Specificity of the interaction of amino-and carboxy-terminal fragments of the mitochondrial precursor protein apocytochrome c with negatively charged phospholipids. A spin-label electron spin resonance study. Biochemistry 28: 8998–9005
Kleene R, Pfanner N, Pfaller R, Link T, Sebald W, Neupert W, Tropschug M (1987) Mitochondrial porin of Neurospora crassa: cDNA cloning, in vitro expression and import into mitochondria. EMBO J 6: 2627–2633
Mannella C A (1982) Structure of the outer mitochondrial membrane: ordered arrays of porelike subunits in outer-membrane fractions from Neurospora crassa mitochondria. J Cell Biol 94: 680–687
Mannella C A (1984) Phospholipase-induced crystallization of channels in mitochondrial outer membranes. Science 224: 165–166
Mannella C A (1992a) The ins and outs of mitochondrial membrane channels. Trends Biochem Sci, 17: 315–320
Mannella C A (1992b) Model for a gated mitochondrial channel based on electron microscopy of 2D crystal polymorphs. Trans Am Crystal Assn, in press
Mannella C A, Bonner W D, Jr. (1975) X-ray diffraction from oriented outer mitochondrial membranes: Detection of in-plane subunit structure. Biochim Biophys Acta 413: 226–233
Mannella C A, Guo X W (1990) Interaction between the VDAC channel and a polyanionic effector. An electron microscopic study. Biophys J 57: 23–31
Mannella C A, Guo X W, Cognon B (1989) Diameter of the mitochondrial outer membrane channel: evidence from electron microscopy of frozen-hydrated membrane crystals. FEBS Lett 253: 231–234
Mannella C A, Guo X W, Dias J (1992a) Binding of a synthetic targeting peptide to a mitochondrial channel protein. J Bioenerg Biomembr 24: 55–61
Mannella C A, Ribeiro A, Frank J (1986) Structure of the channels in the outer mitochondrial membrane. Biophys J 49: 307–318
Mannella C A, Stanley S, D’Arcangelis D, Dias J A (1992b) Location of the N-terminal region of the channel protein, VDAC, in the outer membrane of Neurospora mitochondria. Biophys J 61: A14
Massalski A, Sass H J, Zemlin F, Beckmann E, van Heel M, Buldt G, Dorset D L, Zeitler E, Rosenbusch J P (1987) High-resolution, low-dose electron cryomicroscopy of negatively stained matrix porin, a transmembrane protein from Escherichia coli outer membranes. In: Proc. 45th Annual Meeting of the Electron Microscopy Society of America. Bailey G W (ed) San Francisco Press, Inc. San Francisco, p. 788–789
Mohraz M, Yee M, Smith P R (1985) Novel crystalline sheets of Na, K-ATPase induced by phospholipase A2. J Ultrastruct Res 93: 17–26
Roise D, Horvath S J, Tomich J M, Richards J H, Schatz G (1986) A chemically synthesized pre-sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers. EMBO J 5: 1327–1334
Tamm L K (1991) Membrane insertion and lateral mobility of synthetic amphiphilic signal peptides in lipid model membranes. Biochim Biophys Acta 1071: 123–148
Thomas L, Kocsis E, Colombini M, Erbe E, Trus B L, Steven A C (1991) Surface topography and molecular stoichiometry of the mitochondrial channel, VDAC, in crystalline arrays. J Struct Biol 106: 161–171
Weiss M S, Kreusch A, Schiltz E, Nestel U, Weite W, Weckesser J, Schulz G E (1991) The structure of porin from Rhodobacter capsulata at 1.8 A resolution. FEBS Lett 280: 379–382
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1994 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
Mannella, C.A. (1994). Insights Into the Structure of the Mitochondrial Channel, VDAC, Provided by Electron Microscopy. In: Forte, M., Colombini, M. (eds) Molecular Biology of Mitochondrial Transport Systems. NATO ASI Series, vol 83. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78936-6_18
Download citation
DOI: https://doi.org/10.1007/978-3-642-78936-6_18
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-78938-0
Online ISBN: 978-3-642-78936-6
eBook Packages: Springer Book Archive